AROQ_ACIBT
ID AROQ_ACIBT Reviewed; 151 AA.
AC A3M692;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=3-dehydroquinate dehydratase {ECO:0000255|HAMAP-Rule:MF_00169};
DE Short=3-dehydroquinase {ECO:0000255|HAMAP-Rule:MF_00169};
DE EC=4.2.1.10 {ECO:0000255|HAMAP-Rule:MF_00169};
DE AltName: Full=Type II DHQase {ECO:0000255|HAMAP-Rule:MF_00169};
GN Name=aroQ {ECO:0000255|HAMAP-Rule:MF_00169}; OrderedLocusNames=A1S_2009;
OS Acinetobacter baumannii (strain ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC
OS KC755 / 5377).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=400667;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377;
RX PubMed=17344419; DOI=10.1101/gad.1510307;
RA Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N.,
RA Gerstein M., Snyder M.;
RT "New insights into Acinetobacter baumannii pathogenesis revealed by high-
RT density pyrosequencing and transposon mutagenesis.";
RL Genes Dev. 21:601-614(2007).
CC -!- FUNCTION: Catalyzes a trans-dehydration via an enolate intermediate.
CC {ECO:0000255|HAMAP-Rule:MF_00169}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O;
CC Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630,
CC ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00169};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 3/7. {ECO:0000255|HAMAP-Rule:MF_00169}.
CC -!- SUBUNIT: Homododecamer. {ECO:0000255|HAMAP-Rule:MF_00169}.
CC -!- SIMILARITY: Belongs to the type-II 3-dehydroquinase family.
CC {ECO:0000255|HAMAP-Rule:MF_00169}.
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DR EMBL; CP000521; ABO12436.2; -; Genomic_DNA.
DR RefSeq; WP_000099415.1; NZ_CP053098.1.
DR PDB; 4RC9; X-ray; 2.05 A; A/B/C/D/E/F/G/H/I/J/K/L=1-151.
DR PDB; 4RHC; X-ray; 2.68 A; A/B/C/D/E/F/G/H/I/J/K/L=2-151.
DR PDB; 4ZC1; X-ray; 2.52 A; A/B/C/D/E/F/G/H/I/J/K/L=1-146.
DR PDB; 5B6P; X-ray; 2.00 A; A/B/C/D/E/F/G/H/I/J/K/L=1-151.
DR PDB; 5WRF; X-ray; 2.51 A; A/B/C/D/E/F/G/H/I/J/K/L=2-146.
DR PDB; 5X47; X-ray; 2.54 A; A/B/C/D/E/F/G/H/I/J/K/L=2-146.
DR PDB; 5YDB; X-ray; 1.76 A; A/B/C/D=3-150.
DR PDB; 5YHM; X-ray; 1.91 A; A/B/C/D/E/F/G/H/I/J/K/L=3-147.
DR PDB; 5YL5; X-ray; 1.90 A; A/B/C/D/E/F/G/H/I/J/K/L=1-151.
DR PDB; 5YPQ; X-ray; 2.65 A; A/B/C/D/E/F/G/H/I/J/K/L=1-151.
DR PDBsum; 4RC9; -.
DR PDBsum; 4RHC; -.
DR PDBsum; 4ZC1; -.
DR PDBsum; 5B6P; -.
DR PDBsum; 5WRF; -.
DR PDBsum; 5X47; -.
DR PDBsum; 5YDB; -.
DR PDBsum; 5YHM; -.
DR PDBsum; 5YL5; -.
DR PDBsum; 5YPQ; -.
DR AlphaFoldDB; A3M692; -.
DR SMR; A3M692; -.
DR KEGG; acb:A1S_2009; -.
DR HOGENOM; CLU_090968_1_0_6; -.
DR BRENDA; 4.2.1.10; 98.
DR UniPathway; UPA00053; UER00086.
DR GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00466; DHQase_II; 1.
DR Gene3D; 3.40.50.9100; -; 1.
DR HAMAP; MF_00169; AroQ; 1.
DR InterPro; IPR001874; DHquinase_II.
DR InterPro; IPR018509; DHquinase_II_CS.
DR InterPro; IPR036441; DHquinase_II_sf.
DR PANTHER; PTHR21272; PTHR21272; 1.
DR Pfam; PF01220; DHquinase_II; 1.
DR PIRSF; PIRSF001399; DHquinase_II; 1.
DR SUPFAM; SSF52304; SSF52304; 1.
DR TIGRFAMs; TIGR01088; aroQ; 1.
DR PROSITE; PS01029; DEHYDROQUINASE_II; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Lyase.
FT CHAIN 1..151
FT /note="3-dehydroquinate dehydratase"
FT /id="PRO_1000097587"
FT ACT_SITE 24
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT ACT_SITE 102
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT BINDING 76
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT BINDING 82
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT BINDING 89
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT BINDING 103..104
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT BINDING 113
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT SITE 19
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00169"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:5YDB"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:5YDB"
FT TURN 16..18
FT /evidence="ECO:0007829|PDB:5YDB"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:5YDB"
FT HELIX 29..42
FT /evidence="ECO:0007829|PDB:5YDB"
FT STRAND 47..51
FT /evidence="ECO:0007829|PDB:5YDB"
FT HELIX 55..67
FT /evidence="ECO:0007829|PDB:5YDB"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:5YDB"
FT HELIX 78..82
FT /evidence="ECO:0007829|PDB:5YDB"
FT HELIX 85..94
FT /evidence="ECO:0007829|PDB:5YDB"
FT STRAND 98..104
FT /evidence="ECO:0007829|PDB:5YDB"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:5YDB"
FT HELIX 111..114
FT /evidence="ECO:0007829|PDB:5YDB"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:5YDB"
FT STRAND 122..129
FT /evidence="ECO:0007829|PDB:5YDB"
FT HELIX 132..145
FT /evidence="ECO:0007829|PDB:5YDB"
SQ SEQUENCE 151 AA; 16498 MW; 4831E38E45803CBB CRC64;
MSSTILVIHG PNLNLLGKRE PEVYGHLTLD NINRQLIAQA EQASITLDTF QSNWEGAIVD
RIHQAQTEGV KLIIINPAAL THTSVALRDA LLGVAIPFIE VHLSNVHARE AFRHHSYLSD
KAIGVICGLG AKGYSFALDY AIEKIQPSNP N
